6EK5

Near-atomic resolution structure of a plant geminivirus determined by electron cryo-microscopy.

これはPDB形式変換不可エントリーです。

「5MJF」から置き換えられました

6EK5 の概要

• エントリーDOI: 10.2210/pdb6ek5/pdb
• EMDBエントリー: 3521
• 分子名称: Capsid protein (1 entity in total)
• 機能のキーワード: african cassava mosaic virus, geminivirus, acmv, virus
• 由来する生物種: African cassava mosaic virus (ACMV)
• タンパク質・核酸の鎖数: 110
• 化学式量合計: 2650438.01

構造登録者

Grimm, C.,Bottcher, B.,Hipp, K.,Jeske, H. (登録日: 2017-09-25, 公開日: 2017-10-11, 最終更新日: 2024-07-10)

主引用文献

Hipp, K.,Grimm, C.,Jeske, H.,Bottcher, B.
Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy.
Structure, 25:1303-1309.e3, 2017

PubMed Abstract: African cassava mosaic virus is a whitefly-transmitted geminivirus which forms unique twin particles of incomplete icosahedra that are joined at five-fold vertices, building an unusual waist. How its 22 capsomers interact within a half-capsid or across the waist is unknown thus far. Using electron cryo-microscopy and image processing, we determined the virion structure with a resolution of 4.2 Å and built an atomic model for its capsid protein. The inter-capsomer contacts mediated by the flexible N termini and loop regions differed within the half-capsids and at the waist, explaining partly the unusual twin structure. The tip of the pentameric capsomer is sealed by a plug formed by a turn region harboring the evolutionary conserved residue Y193. Basic amino acid residues inside the capsid form a positively charged pocket next to the five-fold axis of the capsomer suitable for binding DNA. Within this pocket, density most likely corresponding to DNA was resolved.

PubMed: 28712809
DOI: 10.1016/j.str.2017.06.013

実験手法

ELECTRON MICROSCOPY (4.2 Å)